Which of the following statements are correct about protein folding (select all that appy)? A. Protein folding is a very slow process with most proteins requiring >30 min to go from unfolded to native conformation B. The mature two-chain form of insulin spontaneously folds into the native conformation C. A sharp transition in the presence of denaturants (See Figue 8.1) suggests the protein folds without intermediates D. Proteins randomly sample each possible conformation before arriving final native state E. Proteins with disulfide bridges tend not follow a simple two-state folding mechanism.

Which of the following statements are correct about protein folding (select all that appy)? A. Protein folding is a very slow process with most proteins requiring >30 min to go from unfolded to native conformation B. The mature two-chain form of insulin spontaneously folds into the native conformation C. A sharp transition in the presence of denaturants (See Figue 8.1) suggests the protein folds without intermediates D. Proteins randomly sample each possible conformation before arriving final native state E. Proteins with disulfide bridges tend not follow a simple two-state folding mechanism.

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter4: Cells

Section: Chapter Questions

Problem 1ITD

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Which of the following statements are correct about the role of chaperones in protein folding (select all that appy)? A. Chaperones accelerate the rate of protein folding B. Presence of chaperones contradicts dogma that structure of protein is only determined by amino acid sequence C. Chapreone promotion of native folding is an ATP-dependent process D. Chaperones work by stabilizing hydrophobic patches on proteins E. A cell line with the GroEL and GroES deleted would accumulate more unfolded protein
A certain protein is used to activate myosin. If the protein is treated with B-mercaptoethanol, it will not activate myosin. What can you say about the structure of this protein? O The peptide is denatured by B-mercaptoethanol O The peptide does not have a thermodynamically stable configuration O The peptide contains more than one distinct chain O The peptide contains disulfide bonds required for activity
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	A.	Protein folding is a very slow process with most proteins requiring >30 min to go from unfolded to native conformation
	B.	The mature two-chain form of insulin spontaneously folds into the native conformation
	C.	A sharp transition in the presence of denaturants (See Figue 8.1) suggests the protein folds without intermediates
	D.	Proteins randomly sample each possible conformation before arriving final native state
	E.	Proteins with disulfide bridges tend not follow a simple two-state folding mechanism.